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Conserved domains on  [gi|459215038|ref|NP_001264006|]
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homer protein homolog 1 isoform 2 [Homo sapiens]

Protein Classification

Homer/Vesl family EVH1 domain-containing protein( domain architecture ID 10100433)

Homer/Vesl family EVH1 (WH1, RanBP1-WASP) domain-containing protein is a synaptic scaffolding protein, required for long-term potentiation, a form of synaptic plasticity thought to underlie memory formation

CATH:  2.30.29.30
Gene Ontology:  GO:0007216|GO:0035256|GO:0005515
PubMed:  11911879|17316461
SCOP:  4002440

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EVH1_Homer_Vesl cd01206
Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, ...
 3-101 1.10e-73

Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, required for long-term potentiation, a form of synaptic plasticity thought to underlie memory formation. They contains an N-terminal EVH1 domain and bind to both neurotransmitter receptors, such as the metabotropic group 1 glutamate receptor (mGluR) and to other scaffolding proteins via PPXXF motifs, in order to target them to the synaptic junction. These mGluRs possess a long C-terminal intracellular tail that may be important for subcellular localization of the receptor. The C-terminus is also the site of binding by the immediate early gene (IEG), Homer 1a. In contrast to Homer 1a, other Homer members additionally encode a C-terminal coiled-coil (CC) domain and form multivalent complexes that bind group 1 mGluRs. Homer 1a competes with constitutively expressed CC-Homers to modify the association of group 1 mGluRs with CC-Homer complexes. Since Homer proteins are strikingly enriched at the postsynaptic density (PSD), these observations suggest a role for the Homer family in regulating synaptic metabotropic receptor function. PSD-Zip45 (also named Homer 1c/Vesl-1L) has an EVH1 domain with a longer alpha-helix and its linking part included in the conserved region of Homer 1 (CRH1) interacts with the EVH1 domain of the neighbour CRH1 molecule in the crystal, suggesting that the EVH1 domain recognizes the PPXXF motif found in the binding partners, and the SPLTP sequence (P-motif) in the linking region of the CRH1. The two types of binding are partly overlapped in the EVH1 domain, implying a mechanism to regulate multimerization of Homer 1 family proteins. Homer 2 and Homer 3 are negative regulators of T cell activation. They bind the nuclear factor of activated T cells (NFAT) and compete with calcineurin binding. NFAT plays a critical role in calcium-dependent signaling in other cell types, including muscle and neurons. Homer-NFAT binding is also antagonized by active serine-threonine kinase AKT, enhancing TCR signaling via calcineurin-dependent dephosphorylation of NFAT resulting in changes in cytokine expression and an increase in effector-memory T cell populations in Homer-deficient mice. The EVH1 domains are part of the PH domain superamily. There are 5 EVH1 subfamilies: Enables/VASP, Homer/Vesl, WASP, Dcp1, and Spred. Ligands are known for three of the EVH1 subfamilies, all of which bind proline-rich sequences: the Enabled/VASP family binds to FPPPP peptides, the Homer/Vesl family binds PPxxF peptides, and the WASP family binds LPPPEP peptides. EVH1 has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains.


:

Pssm-ID: 269917  Cd Length: 109  Bit Score: 218.37  E-value: 1.10e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038   3 EQPIFSTRAHVFQIDPNTKKNWVPTSKHAVTVSYFYDSTRNVYRIISLDGSKAIINSTITPNMTFTKTSQKFGQWADSRA 82
Cdd:cd01206    1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                         90
                 ....*....|....*....
gi 459215038  83 NTVYGLGFSSEHHLSKVTE 101
Cdd:cd01206   81 NTVYGLGFASEAELTKFAE 99
PRK12704 super family cl36166
phosphodiesterase; Provisional
 137-222 4.83e-07

phosphodiesterase; Provisional


The actual alignment was detected with superfamily member PRK12704:

Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 49.78  E-value: 4.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038 137 IERLKQEIDnaRELQEQRdsltQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFELTELRDN 216
Cdd:PRK12704  66 IHKLRNEFE--KELRERR----NELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE 139


                 ....*.
gi 459215038 217 LAKLLE 222
Cdd:PRK12704 140 QLQELE 145
 
Name Accession Description Interval E-value
EVH1_Homer_Vesl cd01206
Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, ...
 3-101 1.10e-73

Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, required for long-term potentiation, a form of synaptic plasticity thought to underlie memory formation. They contains an N-terminal EVH1 domain and bind to both neurotransmitter receptors, such as the metabotropic group 1 glutamate receptor (mGluR) and to other scaffolding proteins via PPXXF motifs, in order to target them to the synaptic junction. These mGluRs possess a long C-terminal intracellular tail that may be important for subcellular localization of the receptor. The C-terminus is also the site of binding by the immediate early gene (IEG), Homer 1a. In contrast to Homer 1a, other Homer members additionally encode a C-terminal coiled-coil (CC) domain and form multivalent complexes that bind group 1 mGluRs. Homer 1a competes with constitutively expressed CC-Homers to modify the association of group 1 mGluRs with CC-Homer complexes. Since Homer proteins are strikingly enriched at the postsynaptic density (PSD), these observations suggest a role for the Homer family in regulating synaptic metabotropic receptor function. PSD-Zip45 (also named Homer 1c/Vesl-1L) has an EVH1 domain with a longer alpha-helix and its linking part included in the conserved region of Homer 1 (CRH1) interacts with the EVH1 domain of the neighbour CRH1 molecule in the crystal, suggesting that the EVH1 domain recognizes the PPXXF motif found in the binding partners, and the SPLTP sequence (P-motif) in the linking region of the CRH1. The two types of binding are partly overlapped in the EVH1 domain, implying a mechanism to regulate multimerization of Homer 1 family proteins. Homer 2 and Homer 3 are negative regulators of T cell activation. They bind the nuclear factor of activated T cells (NFAT) and compete with calcineurin binding. NFAT plays a critical role in calcium-dependent signaling in other cell types, including muscle and neurons. Homer-NFAT binding is also antagonized by active serine-threonine kinase AKT, enhancing TCR signaling via calcineurin-dependent dephosphorylation of NFAT resulting in changes in cytokine expression and an increase in effector-memory T cell populations in Homer-deficient mice. The EVH1 domains are part of the PH domain superamily. There are 5 EVH1 subfamilies: Enables/VASP, Homer/Vesl, WASP, Dcp1, and Spred. Ligands are known for three of the EVH1 subfamilies, all of which bind proline-rich sequences: the Enabled/VASP family binds to FPPPP peptides, the Homer/Vesl family binds PPxxF peptides, and the WASP family binds LPPPEP peptides. EVH1 has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains.


Pssm-ID: 269917  Cd Length: 109  Bit Score: 218.37  E-value: 1.10e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038   3 EQPIFSTRAHVFQIDPNTKKNWVPTSKHAVTVSYFYDSTRNVYRIISLDGSKAIINSTITPNMTFTKTSQKFGQWADSRA 82
Cdd:cd01206    1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                         90
                 ....*....|....*....
gi 459215038  83 NTVYGLGFSSEHHLSKVTE 101
Cdd:cd01206   81 NTVYGLGFASEAELTKFAE 99
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 4-103 3.34e-36

WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in Wiskott-Aldrich syndrome (WAS). The majority of point mutations occur within the amino- terminal WH1 domain. The metabotropic glutamate receptors mGluR1alpha and mGluR5 bind a protein called homer, which is a WH1 domain homolog. A subset of WH1 domains has been termed a "EVH1" domain and appear to bind a polyproline motif.


Pssm-ID: 395450  Cd Length: 111  Bit Score: 123.33  E-value: 3.34e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038    4 QPIFSTRAHVFQIDPNTKKNWVPTsKHAVTVSYFYDSTRNVYRIISLD--GSKAIINSTITPNMTFTKTSQKFGQWADSR 81
Cdd:pfam00568   9 QTICTAVAQVYLADPDNKRHWIKA-KHSGVVCFVKDSPQNSYFIRLVDiqDGKVIWNQEIYPNMEYNQARPFFHTFADSR 87

                          90       100
                  ....*....|....*....|....*.
gi 459215038   82 AntVYGLGFSSE----HHLSKVTELE 103
Cdd:pfam00568  88 C--VYGLNFASEeeatKFAKAVQEAL 111
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 1-98 1.05e-31

WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains point mutations in the majority of patients with WAS. Unknown function. Ena-like WH1 domains bind polyproline-containing peptides, and that Homer contains a WH1 domain.


Pssm-ID: 214674  Cd Length: 106  Bit Score: 111.68  E-value: 1.05e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038     1 MGEQPIFSTRAHVFQIDPNTKKnWVPTSKH-AVTVSYFYDSTRNVYRIISLDGS-KAIINSTITPNMTFTKTSQKFGQWA 78
Cdd:smart00461   1 LGSQCIILARAVVQLYDADTKK-WVPTGEGgAANLVIDKNQRSYFFRIVGIKGQdKVIWNQELYKNFKYNQATPTFHQWA 79

                           90       100
                   ....*....|....*....|
gi 459215038    79 DsrANTVYGLGFSSEHHLSK 98
Cdd:smart00461  80 D--DKCVYGLNFASEEEAKK 97
PRK12704 PRK12704
phosphodiesterase; Provisional
 137-222 4.83e-07

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 49.78  E-value: 4.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038 137 IERLKQEIDnaRELQEQRdsltQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFELTELRDN 216
Cdd:PRK12704  66 IHKLRNEFE--KELRERR----NELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE 139


                 ....*.
gi 459215038 217 LAKLLE 222
Cdd:PRK12704 140 QLQELE 145
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 111-222 4.82e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 4.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038 111 AVHTHKTELNQTIQELEETLKLKEEEIERLKQEIDNARELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQE 190
Cdd:COG1196  282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361

                         90       100       110
                 ....*....|....*....|....*....|..
gi 459215038 191 AFRNNLKTLLEILDGKIFELTELRDNLAKLLE 222
Cdd:COG1196  362 EAEEALLEAEAELAEAEEELEELAEELLEALR 393
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 138-222 8.21e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 8.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038   138 ERLKQEIDnarELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFELTELRDNL 217
Cdd:TIGR02169  353 DKLTEEYA---ELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAI 429


                   ....*
gi 459215038   218 AKLLE 222
Cdd:TIGR02169  430 AGIEA 434
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 110-220 8.78e-04

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 39.84  E-value: 8.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038  110 NAVHTHKTELNQTIQELEETLKLKEEEIERLKQ-------EIDNARELQEQRDSL-------TQKLQEVEIRNKDLEGQL 175
Cdd:pfam06160 287 KYVEKNLPEIEDYLEHAEEQNKELKEELERVQQsytlnenELERVRGLEKQLEELekrydeiVERLEEKEVAYSELQEEL 366

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 459215038  176 SDLEQRLEKSQNEQEAFRNNLKTL-------LEILDGKIFELTELRDNLAKL 220
Cdd:pfam06160 367 EEILEQLEEIEEEQEEFKESLQSLrkdeleaREKLDEFKLELREIKRLVEKS 418
 
Name Accession Description Interval E-value
EVH1_Homer_Vesl cd01206
Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, ...
 3-101 1.10e-73

Homer/Vesl family proteins EVH1 domain; Homer/Vesl proteins are synaptic scaffolding proteins, required for long-term potentiation, a form of synaptic plasticity thought to underlie memory formation. They contains an N-terminal EVH1 domain and bind to both neurotransmitter receptors, such as the metabotropic group 1 glutamate receptor (mGluR) and to other scaffolding proteins via PPXXF motifs, in order to target them to the synaptic junction. These mGluRs possess a long C-terminal intracellular tail that may be important for subcellular localization of the receptor. The C-terminus is also the site of binding by the immediate early gene (IEG), Homer 1a. In contrast to Homer 1a, other Homer members additionally encode a C-terminal coiled-coil (CC) domain and form multivalent complexes that bind group 1 mGluRs. Homer 1a competes with constitutively expressed CC-Homers to modify the association of group 1 mGluRs with CC-Homer complexes. Since Homer proteins are strikingly enriched at the postsynaptic density (PSD), these observations suggest a role for the Homer family in regulating synaptic metabotropic receptor function. PSD-Zip45 (also named Homer 1c/Vesl-1L) has an EVH1 domain with a longer alpha-helix and its linking part included in the conserved region of Homer 1 (CRH1) interacts with the EVH1 domain of the neighbour CRH1 molecule in the crystal, suggesting that the EVH1 domain recognizes the PPXXF motif found in the binding partners, and the SPLTP sequence (P-motif) in the linking region of the CRH1. The two types of binding are partly overlapped in the EVH1 domain, implying a mechanism to regulate multimerization of Homer 1 family proteins. Homer 2 and Homer 3 are negative regulators of T cell activation. They bind the nuclear factor of activated T cells (NFAT) and compete with calcineurin binding. NFAT plays a critical role in calcium-dependent signaling in other cell types, including muscle and neurons. Homer-NFAT binding is also antagonized by active serine-threonine kinase AKT, enhancing TCR signaling via calcineurin-dependent dephosphorylation of NFAT resulting in changes in cytokine expression and an increase in effector-memory T cell populations in Homer-deficient mice. The EVH1 domains are part of the PH domain superamily. There are 5 EVH1 subfamilies: Enables/VASP, Homer/Vesl, WASP, Dcp1, and Spred. Ligands are known for three of the EVH1 subfamilies, all of which bind proline-rich sequences: the Enabled/VASP family binds to FPPPP peptides, the Homer/Vesl family binds PPxxF peptides, and the WASP family binds LPPPEP peptides. EVH1 has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains.


Pssm-ID: 269917  Cd Length: 109  Bit Score: 218.37  E-value: 1.10e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038   3 EQPIFSTRAHVFQIDPNTKKNWVPTSKHAVTVSYFYDSTRNVYRIISLDGSKAIINSTITPNMTFTKTSQKFGQWADSRA 82
Cdd:cd01206    1 EQPIFTTQAHVFQIDPQTKKSWIPASKQAVTVSFFYDSTRNTYRIISVEGSKAIINSTITPNMTFTKTSQKFGQWADSRA 80

                         90
                 ....*....|....*....
gi 459215038  83 NTVYGLGFSSEHHLSKVTE 101
Cdd:cd01206   81 NTVYGLGFASEAELTKFAE 99
EVH1_family cd00837
EVH1 (Drosophila Enabled (Ena)/Vasodilator-stimulated phosphoprotein (VASP) homology 1) domain; ...
 5-98 5.78e-40

EVH1 (Drosophila Enabled (Ena)/Vasodilator-stimulated phosphoprotein (VASP) homology 1) domain; The EVH1 domains are part of the PH domain superfamily. EVH1 subfamilies include Enables/VASP, Homer/Vesl, WASP, and Spred. Ligands are known for three of the EVH1 subfamilies, all of which bind proline-rich sequences: the Enabled/VASP family binds to FPPPP peptides, the Homer/Vesl family binds PPxxF peptides, and the WASP family binds LPPPEP peptides. EVH1 has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains.


Pssm-ID: 269909  Cd Length: 103  Bit Score: 132.59  E-value: 5.78e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038   5 PIFSTRAHVFQIDPNtKKNWVPTS-KHAVTVSYFYDSTRNVYRIISLDGS--KAIINSTITPNMTFTKTSQKFGQWADSR 81
Cdd:cd00837    1 SIFSARAHVMQIDDS-NKNWVPAGgKGASRVSYFKDTTRNSFRIIGVDIKdkKVVINCTITKNLVYNKATQTFHQWADDR 79

                         90
                 ....*....|....*..
gi 459215038  82 anTVYGLGFSSEHHLSK 98
Cdd:cd00837   80 --TVFGLNFASEEDATK 94
WH1 pfam00568
WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in ...
 4-103 3.34e-36

WH1 domain; WASp Homology domain 1 (WH1) domain. WASP is the protein that is defective in Wiskott-Aldrich syndrome (WAS). The majority of point mutations occur within the amino- terminal WH1 domain. The metabotropic glutamate receptors mGluR1alpha and mGluR5 bind a protein called homer, which is a WH1 domain homolog. A subset of WH1 domains has been termed a "EVH1" domain and appear to bind a polyproline motif.


Pssm-ID: 395450  Cd Length: 111  Bit Score: 123.33  E-value: 3.34e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038    4 QPIFSTRAHVFQIDPNTKKNWVPTsKHAVTVSYFYDSTRNVYRIISLD--GSKAIINSTITPNMTFTKTSQKFGQWADSR 81
Cdd:pfam00568   9 QTICTAVAQVYLADPDNKRHWIKA-KHSGVVCFVKDSPQNSYFIRLVDiqDGKVIWNQEIYPNMEYNQARPFFHTFADSR 87

                          90       100
                  ....*....|....*....|....*.
gi 459215038   82 AntVYGLGFSSE----HHLSKVTELE 103
Cdd:pfam00568  88 C--VYGLNFASEeeatKFAKAVQEAL 111
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 1-98 1.05e-31

WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains point mutations in the majority of patients with WAS. Unknown function. Ena-like WH1 domains bind polyproline-containing peptides, and that Homer contains a WH1 domain.


Pssm-ID: 214674  Cd Length: 106  Bit Score: 111.68  E-value: 1.05e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038     1 MGEQPIFSTRAHVFQIDPNTKKnWVPTSKH-AVTVSYFYDSTRNVYRIISLDGS-KAIINSTITPNMTFTKTSQKFGQWA 78
Cdd:smart00461   1 LGSQCIILARAVVQLYDADTKK-WVPTGEGgAANLVIDKNQRSYFFRIVGIKGQdKVIWNQELYKNFKYNQATPTFHQWA 79

                           90       100
                   ....*....|....*....|
gi 459215038    79 DsrANTVYGLGFSSEHHLSK 98
Cdd:smart00461  80 D--DKCVYGLNFASEEEAKK 97
EVH1_Ena_VASP-like cd01207
Enabled/VASP family EVH1 domain; Ena/VASP family includes proteins such as: ...
 5-93 2.35e-11

Enabled/VASP family EVH1 domain; Ena/VASP family includes proteins such as: Vasodilator-stimulated phosphoprotein (VASP), enabled gene product from Drosophila (Ena), mammalian enabled (Mena) and Ena/VASP-Like protein (EVL) localize to focal adhesions and to sites of actin filament dynamics. These proteins share a common modular organization with a highly conserved N- and C-terminal domains, termed Ena/VASP homology domains 1 and 2 (EVH1 and EVH2), that are separated by a central proline-rich domain. The EVH1 domain binds to other proteins at proline rich sequences. The majority of Ena-VASP type EVH1 domains recognize FPPPP motifs such as in the focal adhesion proteins zyxin and vinculin, and the ActA surface protein of Listeria monocytogenes, however the LIM3 domain of Tes lacks the FPPPP motif but still binds the EVH1 domain of Mena. It has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains. EVH2 mediates oligomerization within the family. The proline-rich region binds SH3 and WW domains as well as profilin, a protein that regulates actin filament dynamics. The EVH1 domains are part of the PH domain superamily. There are 5 EVH1 subfamilies: Enables/VASP, Homer/Vesl, WASP, Dcp1, and Spred. Ligands are known for three of the EVH1 subfamilies, all of which bind proline-rich sequences: the Enabled/VASP family binds to FPPPP peptides, the Homer/Vesl family binds PPxxF peptides, and the WASP family binds LPPPEP peptides. EVH1 has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains.


Pssm-ID: 269918  Cd Length: 108  Bit Score: 58.47  E-value: 2.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038   5 PIFSTRAHVFQIDPNTKKnWVPT-SKHAVTVSYFYDSTR-NVYRIIS--LDGSKAIINSTITPNMTFTKTSQKFGQWADS 80
Cdd:cd01207    1 SVASARASVMVYDDENKR-WVPSgGSQGLSRVQIYHNTRnNTFRVVGrkLQDHEVVINCAILKGLKYNQATPTFHQWRDA 79

                         90
                 ....*....|...
gi 459215038  81 RanTVYGLGFSSE 93
Cdd:cd01207   80 R--QVYGLNFASK 90
PRK12704 PRK12704
phosphodiesterase; Provisional
 137-222 4.83e-07

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 49.78  E-value: 4.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038 137 IERLKQEIDnaRELQEQRdsltQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFELTELRDN 216
Cdd:PRK12704  66 IHKLRNEFE--KELRERR----NELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE 139


                 ....*.
gi 459215038 217 LAKLLE 222
Cdd:PRK12704 140 QLQELE 145
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 111-222 4.82e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 4.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038 111 AVHTHKTELNQTIQELEETLKLKEEEIERLKQEIDNARELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQE 190
Cdd:COG1196  282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361

                         90       100       110
                 ....*....|....*....|....*....|..
gi 459215038 191 AFRNNLKTLLEILDGKIFELTELRDNLAKLLE 222
Cdd:COG1196  362 EAEEALLEAEAELAEAEEELEELAEELLEALR 393
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 105-203 7.99e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.83  E-value: 7.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038 105 VSSQANAVHTHKTELNQTIQELEETLklkeeeiERLKQEIDNARELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEK 184
Cdd:COG4942   15 AAAQADAAAEAEAELEQLQQEIAELE-------KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87

                         90
                 ....*....|....*....
gi 459215038 185 SQNEQEAFRNNLKTLLEIL 203
Cdd:COG4942   88 LEKEIAELRAELEAQKEEL 106
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 138-222 8.21e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 8.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038   138 ERLKQEIDnarELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFELTELRDNL 217
Cdd:TIGR02169  353 DKLTEEYA---ELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAI 429


                   ....*
gi 459215038   218 AKLLE 222
Cdd:TIGR02169  430 AGIEA 434
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 137-222 8.79e-05

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.22  E-value: 8.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038 137 IERLKQEIDnarELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNN------------LKTLLEILD 204
Cdd:COG1579   33 LAELEDELA---ALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeyealqkeiesLKRRISDLE 109

                         90
                 ....*....|....*...
gi 459215038 205 GKIFELTELRDNLAKLLE 222
Cdd:COG1579  110 DEILELMERIEELEEELA 127
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 99-222 1.21e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038  99 VTELECVSSQANAVHTHKTELNQTIQELEETLKLKEEEIERLKQEIDNARE----LQEQRDSLTQKLQEVEIRNKDLEGQ 174
Cdd:COG1196  259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEErrreLEERLEELEEELAELEEELEELEEE 338

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 459215038 175 LSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFELTELRDNLAKLLE 222
Cdd:COG1196  339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 101-222 1.35e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.83  E-value: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038 101 ELECVSSQANAVHTHKTELNQTIQELEETLKLKEEEIERLKQ---EIDNARELQ----------EQRDSLTQKLQEVEIR 167
Cdd:COG1579   39 ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgNVRNNKEYEalqkeieslkRRISDLEDEILELMER 118

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 459215038 168 NKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFELTELRDNLAKLLE 222
Cdd:COG1579  119 IEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 138-203 2.10e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 2.10e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 459215038   138 ERLKQEIDNARELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEIL 203
Cdd:TIGR02168  880 NERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 100-222 2.68e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 2.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038   100 TELECVSSQANAVHTHKTELNQTIQELEETLKLKEEEIERLKQEIDNARE----LQEQRDSLTQKLQEVEIRNKDLEGQL 175
Cdd:TIGR02168  698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEEriaqLSKELTELEAEIEELEERLEEAEEEL 777

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 459215038   176 SDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFELTELRDNLAKLLE 222
Cdd:TIGR02168  778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
137-218 3.95e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 3.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038  137 IERLKQEIDNA-------RELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILD-GKIF 208
Cdd:COG4913   670 IAELEAELERLdassddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlELRA 749

                          90
                  ....*....|
gi 459215038  209 ELTELRDNLA 218
Cdd:COG4913   750 LLEERFAAAL 759
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 95-222 4.46e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 4.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038    95 HLSKVTELECVSSQANAVHTHKTELNQTIQELEETLKLKEEEIERLKQEIdnaRELQEQRDSLTQKLQEVEIRNKDLEGQ 174
Cdd:TIGR02168  255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK---QILRERLANLERQLEELEAQLEELESK 331

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 459215038   175 LSDLEQRLEKSQNEQEAFRNNLKTLLEILD---GKIFELTELRDNLAKLLE 222
Cdd:TIGR02168  332 LDELAEELAELEEKLEELKEELESLEAELEeleAELEELESRLEELEEQLE 382
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
137-222 5.53e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 5.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038  137 IERLKQEIDNAR----ELQEQRDSLTQKLQEVEIRNKD-LEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFELT 211
Cdd:COG4913   304 LARLEAELERLEarldALREELDELEAQIRGNGGDRLEqLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFA 383

                          90
                  ....*....|.
gi 459215038  212 ELRDNLAKLLE 222
Cdd:COG4913   384 ALRAEAAALLE 394
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 110-222 6.76e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 6.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038   110 NAVHTHKTELNQTIQELEETLKLKEEEIERLKQEIDNareLQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQR-------- 181
Cdd:TIGR02169  822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN---LNGKKEELEEELEELEAALRDLESRLGDLKKErdeleaql 898

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 459215038   182 --LEKSQNEQEA----FRNNLKTLLEILDGKIFELTELRDNLAKLLE 222
Cdd:TIGR02169  899 reLERKIEELEAqiekKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 116-222 7.39e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 7.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038 116 KTELNQTIQELEETLKLKEEEIERLKQEIDNARELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNN 195
Cdd:COG1196  350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429

                         90       100
                 ....*....|....*....|....*..
gi 459215038 196 LKTLLEILDGKIFELTELRDNLAKLLE 222
Cdd:COG1196  430 LAELEEEEEEEEEALEEAAEEEAELEE 456
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 137-220 7.94e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 7.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038 137 IERLKQEIDnarELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFELTELRDN 216
Cdd:COG4942   22 AAEAEAELE---QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98


                 ....
gi 459215038 217 LAKL 220
Cdd:COG4942   99 LEAQ 102
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 110-220 8.78e-04

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 39.84  E-value: 8.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038  110 NAVHTHKTELNQTIQELEETLKLKEEEIERLKQ-------EIDNARELQEQRDSL-------TQKLQEVEIRNKDLEGQL 175
Cdd:pfam06160 287 KYVEKNLPEIEDYLEHAEEQNKELKEELERVQQsytlnenELERVRGLEKQLEELekrydeiVERLEEKEVAYSELQEEL 366

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 459215038  176 SDLEQRLEKSQNEQEAFRNNLKTL-------LEILDGKIFELTELRDNLAKL 220
Cdd:pfam06160 367 EEILEQLEEIEEEQEEFKESLQSLrkdeleaREKLDEFKLELREIKRLVEKS 418
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 101-222 1.10e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038 101 ELECVSSQANAVHTHKTELNQTIQELEETLKLKEEEIERLKQEIDNA----RELQEQRDSLTQKLQEVEIRNKDLEGQLS 176
Cdd:COG1196  240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeeYELLAELARLEQDIARLEERRRELEERLE 319

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 459215038 177 DLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFELTELRDNLAKLLE 222
Cdd:COG1196  320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 92-220 1.17e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 39.49  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038   92 SEHHLSKVTELECVSSQANAVHTHKTELNQTIQELEETLKLKEEEIERLKQEIDNARELQEQRDSLTQKLQEV------- 164
Cdd:pfam07888 142 TQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTittltqk 221

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 459215038  165 -------EIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFELTELRDNLAKL 220
Cdd:pfam07888 222 lttahrkEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQL 284
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
137-222 1.17e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038  137 IERLKQEIDnarELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAfrnNLKTLLEILDGKIFELTELRDN 216
Cdd:COG4913   290 LELLEAELE---ELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLE---QLEREIERLERELEERERRRAR 363


                  ....*.
gi 459215038  217 LAKLLE 222
Cdd:COG4913   364 LEALLA 369
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 100-222 1.22e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038 100 TELECVSSQANAVHTHKTELNQTIQELEETLKLKEEEIERLKQEIDnarELQEQRDSLTQKLQEVEIRNKDLEGQLSDLE 179
Cdd:COG1196  253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA---RLEQDIARLEERRRELEERLEELEEELAELE 329

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 459215038 180 QRLEKSQNEQEAFRNNLKTLLEILDGKIFELTELRDNLAKLLE 222
Cdd:COG1196  330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
 137-212 1.83e-03

Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.


Pssm-ID: 463102 [Multi-domain]  Cd Length: 140  Bit Score: 37.28  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038  137 IERLKQEIDNARE-----------LQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDG 205
Cdd:pfam10473  54 VETLKAEIEEMAQnlrdleldlvtLRSEKENLTKELQKKQERVSELESLNSSLENLLEEKEQEKVQMKEESKTAVEMLQT 133


                  ....*..
gi 459215038  206 KIFELTE 212
Cdd:pfam10473 134 QLKELNE 140
Knl1_RWD_C pfam18210
Knl1 RWD C-terminal domain; This domain is found in Knl1, a sub-unit of the KMN network, ...
 149-220 2.40e-03

Knl1 RWD C-terminal domain; This domain is found in Knl1, a sub-unit of the KMN network, present in Homo sapiens. The KMN network is the core of the outer kinetochore which is responsible for microtubule binding/stabilization and controls the spindle assembly checkpoint. This domain is the second of two RING finger, WD repeat, DEAD-like helicase (RWD) domains. The tandem RWD domains mediate kinetochore targeting of the microtubule-binding subunits by interacting with the Mis12 complex. The Mis12 complex is a KMN sub-complex that tethers directly onto the underlying chromatin layer.


Pssm-ID: 465680 [Multi-domain]  Cd Length: 152  Bit Score: 37.05  E-value: 2.40e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 459215038  149 ELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRnnLKTLLEILDGK-IFELTELRDNLAKL 220
Cdd:pfam18210   1 ELKEELEELEEKLEELEERKQELLAAIGEAERIREECWTSEEVLR--LKEELEALESLhGWRITEVSDDTLVF 71
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 116-222 2.77e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.38  E-value: 2.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038 116 KTELNQTIQELEETLKLKEEEIERLKQEIDNA-----------RELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEK 184
Cdd:COG1196  311 RRELEERLEELEEELAELEEELEELEEELEELeeeleeaeeelEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 459215038 185 SQNEQEAFRNNLKTLLEILDGKIFELTELRDNLAKLLE 222
Cdd:COG1196  391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 118-222 3.57e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 37.99  E-value: 3.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038 118 ELNQTIQELEETLKLKEEEIERLKQEIDNARE----LQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFR 193
Cdd:COG1196  299 RLEQDIARLEERRRELEERLEELEEELAELEEeleeLEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378

                         90       100
                 ....*....|....*....|....*....
gi 459215038 194 NNLKTLLEILDGKIFELTELRDNLAKLLE 222
Cdd:COG1196  379 EELEELAEELLEALRAAAELAAQLEELEE 407
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 113-223 4.39e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 37.73  E-value: 4.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038   113 HTHKTELNQTIQELEETLKLKEEEIERLKQEIDNAR----ELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNE 188
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLEELRlevsELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 459215038   189 QEAFRNNLKTLLEILDGKIFELTELRDNLAKLLEC 223
Cdd:TIGR02168  318 LEELEAQLEELESKLDELAEELAELEEKLEELKEE 352
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 137-215 4.51e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 37.88  E-value: 4.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038 137 IERLkqeIDNARELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQE-AFRNNLKTLLEILDGKIFELTELRD 215
Cdd:PRK00409 522 IASL---EELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEkEAQQAIKEAKKEADEIIKELRQLQK 598
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 137-222 5.36e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 37.37  E-value: 5.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038 137 IERLKQEIDNARElqEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRnNLKTLLEILDGKIFELTELRDN 216
Cdd:COG0542  420 LEQLEIEKEALKK--EQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQ-ELKEELEQRYGKIPELEKELAE 496


                 ....*.
gi 459215038 217 LAKLLE 222
Cdd:COG0542  497 LEEELA 502
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
88-218 6.02e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 37.59  E-value: 6.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038   88 LGFSSEHHL-SKVTELECVSSQANAVHTHKTELNQTIQELEETLKLKEEEIERLKQEIDNA------RELQEQRDSLTQ- 159
Cdd:COG4913   604 LGFDNRAKLaALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAsaereiAELEAELERLDAs 683

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 459215038  160 --KLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEildgkifELTELRDNLA 218
Cdd:COG4913   684 sdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE-------ELDELQDRLE 737
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 137-219 6.67e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 37.12  E-value: 6.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038 137 IERLKQEIDnarELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFELTELRDN 216
Cdd:COG3883  135 LEELKADKA---ELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211


                 ...
gi 459215038 217 LAK 219
Cdd:COG3883  212 AAA 214
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
101-217 6.74e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 37.33  E-value: 6.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038 101 ELECVSSQANAVHTHKTELNQTIQELEETLKLKEEEIERLKQEIDN----ARELQEQRDSLTQKLQ--EVEIRNK----- 169
Cdd:PRK02224 308 DAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDleerAEELREEAAELESELEeaREAVEDRreeie 387

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 459215038 170 DLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFELTELRDNL 217
Cdd:PRK02224 388 ELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATL 435
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
137-214 7.66e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 36.97  E-value: 7.66e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 459215038 137 IERLKQEIDNARELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEksqnEQEAFRNNLKTLLEILDGKIFELTELR 214
Cdd:PRK03918 216 LPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIR----ELEERIEELKKEIEELEEKVKELKELK 289
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 138-204 7.79e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 36.73  E-value: 7.79e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 459215038 138 ERLKQEIDNARELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILD 204
Cdd:COG3883   23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 138-220 9.20e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 36.97  E-value: 9.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038   138 ERLKQEIDnarELQEQRDSLTQKLQEVE-------IRNKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTLLEILDGKIFEL 210
Cdd:TIGR02169  677 QRLRERLE---GLKRELSSLQSELRRIEnrldelsQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753

                           90
                   ....*....|
gi 459215038   211 TELRDNLAKL 220
Cdd:TIGR02169  754 ENVKSELKEL 763
mukB PRK04863
chromosome partition protein MukB;
140-224 9.44e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 36.86  E-value: 9.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038  140 LKQEIDNARELQEQRDSLTQKLQEVEIRNKDLEGQLSDLEQRLEKSQNEQEAF---RNNLKTLLEILDGKIFELT----- 211
Cdd:PRK04863  525 LEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEArerRMALRQQLEQLQARIQRLAarapa 604

                          90
                  ....*....|....*
gi 459215038  212 --ELRDNLAKLLECS 224
Cdd:PRK04863  605 wlAAQDALARLREQS 619
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
137-216 9.73e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 36.53  E-value: 9.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459215038 137 IERLKQEIDNARE-LQEQRDSLTQKLQEVEIR----------------NKDLEGQLSDLEQRLEKSQNEQEAFRNNLKTL 199
Cdd:COG3206  166 LELRREEARKALEfLEEQLPELRKELEEAEAAleefrqknglvdlseeAKLLLQQLSELESQLAEARAELAEAEARLAAL 245

                         90
                 ....*....|....*..
gi 459215038 200 LEILDGKIFELTELRDN 216
Cdd:COG3206  246 RAQLGSGPDALPELLQS 262
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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